NGLY1_CHICK
ID NGLY1_CHICK Reviewed; 651 AA.
AC Q5ZJM3;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase;
DE Short=PNGase;
DE EC=3.5.1.52;
DE AltName: Full=N-glycanase 1;
DE AltName: Full=Peptide:N-glycanase;
GN Name=NGLY1; ORFNames=RCJMB04_17c15;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Specifically deglycosylates the denatured form of N-linked
CC glycoproteins in the cytoplasm and assists their proteasome-mediated
CC degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the
CC glycan and the amide side chain of Asn, converting Asn to Asp. Prefers
CC proteins containing high-mannose over those bearing complex type
CC oligosaccharides. Can recognize misfolded proteins in the endoplasmic
CC reticulum that are exported to the cytosol to be destroyed and
CC deglycosylate them, while it has no activity toward native proteins.
CC Deglycosylation is a prerequisite for subsequent proteasome-mediated
CC degradation of some, but not all, misfolded glycoproteins (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine
CC residue in which the glucosamine residue may be further glycosylated,
CC to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a
CC peptide containing an aspartate residue.; EC=3.5.1.52;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transglutaminase-like superfamily. PNGase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00731}.
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DR EMBL; AJ720411; CAG32070.1; -; mRNA.
DR RefSeq; NP_001026159.1; NM_001030988.1.
DR AlphaFoldDB; Q5ZJM3; -.
DR SMR; Q5ZJM3; -.
DR STRING; 9031.ENSGALP00000018418; -.
DR PaxDb; Q5ZJM3; -.
DR GeneID; 420655; -.
DR KEGG; gga:420655; -.
DR CTD; 55768; -.
DR VEuPathDB; HostDB:geneid_420655; -.
DR eggNOG; KOG0909; Eukaryota.
DR InParanoid; Q5ZJM3; -.
DR OrthoDB; 917526at2759; -.
DR PhylomeDB; Q5ZJM3; -.
DR PRO; PR:Q5ZJM3; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000224; F:peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity; IBA:GO_Central.
DR GO; GO:0006516; P:glycoprotein catabolic process; ISS:UniProtKB.
DR GO; GO:0006517; P:protein deglycosylation; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR Gene3D; 2.60.120.1020; -; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR038680; PAW_sf.
DR InterPro; IPR006588; Peptide_N_glycanase_PAW_dom.
DR InterPro; IPR036339; PUB-like_dom_sf.
DR InterPro; IPR018997; PUB_domain.
DR InterPro; IPR002931; Transglutaminase-like.
DR Pfam; PF04721; PAW; 1.
DR Pfam; PF09409; PUB; 1.
DR Pfam; PF01841; Transglut_core; 1.
DR SMART; SM00613; PAW; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF143503; SSF143503; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51398; PAW; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..651
FT /note="Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine
FT amidase"
FT /id="PRO_0000248975"
FT DOMAIN 29..90
FT /note="PUB"
FT DOMAIN 450..651
FT /note="PAW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00731"
FT ACT_SITE 305
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 332
FT /evidence="ECO:0000250"
FT ACT_SITE 349
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 651 AA; 73903 MW; 52C97F97E3BC45E6 CRC64;
MAGSAGLSSS PSSPAVRELC KNARDTFLEA SRLLLTYADN ILRNPYEEKY RSIRNGNPAF
STRLLPVRGA VECLFEMGFQ EGETHMVFPK EASIEQLRKV RDLIAVERSS RLNESNQVHR
SASSETVAIT QAIAHQPSRP AGSVPTPDHQ QPEPSLLQSL KMAADILTTL QSKCDHLILA
YESTSLQQKA LALIPLQQLK EKAQRKLAQA TRLDKGEHVN EEDFLLLELL NWFKNDFFHW
VDNLPCSRCG GQTEGKRDYL SPTDDDLRWN ADRVENHYCS QCQFCNRFPR YNNPEKLLET
RRGRCGEWAN CFTLCCRAVG FEARYVRDWT DHVWTEVYSA SQKRWLHCDP CENVCDKPLL
YEIGWGKKLS YVIAFSKDEV VDVTWRYSCK HQEVLTRRTA LSEAKLRETI NAINKKKQQS
LSEGRRKELL ERTIVELAEF ISPKTPKPGE FGGRTSGSMA WRIARGETGS EERKEVIFIP
SEKEKASKLF HLMYNVVEDS YTRISNNNEQ ITGWGTGIWK AESIARKVET DWKMVYLARK
EGSSSASISW KFECKSVGLK IDNISIRTSS QTFHSGRIKW RLYSPTAEVI LVGDNSLSSY
SDFCGATEVT LEATLSGGDG KAAWQHTQLF RNSLAGCGEN CLEMIIKLAD L
